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Vol. 53, Issue 3, 429-437, March 1998
Department of Pharmacology, Georgetown University School of
Medicine, Washington, D.C. 20007
The N-methyl-D-aspartate (NMDA) receptor is
assembled using proteins from two gene families, NR1 and NR2. Although
a few studies have examined the composition of NMDA receptors
containing NR1, NR2A, and NR2B, the composition of native NMDA
receptors that incorporate the NR2D subunit is not known. The goal of
the current study was to examine the subunit composition of native NMDA
receptors that contain the NR2D subunit in the rat central nervous
system by immunoprecipitation of assembled NMDA receptors from rat
brain tissues using specific antibodies against NR1, NR2A, NR2B, and NR2D subunits. NMDA receptors were solubilized using either
nondenaturing (native) conditions, in which the subunits remain
assembled in complexes, or denaturing conditions, in which the NMDA
subunits are dissociated from one another. Each of the antibodies
selectively and quantitatively immunoprecipitated only the
corresponding subunit when the subunits were solubilized using
denaturing conditions. In contrast, when NMDA receptors were
solubilized under nondenaturing conditions, immunoprecipitation
followed by quantitative immunoblot analysis of the resulting pellets
show that the majority of the NR2D protein is associated with the NR1
subunit. In addition, the NR2D subunit forms a heteromeric assembly
with NR1, as well as with NR2A and/or NR2B subunits, reflecting ternary
complex formation. Finally, a binary complex composed of only NR1/NR2D subunits was found in the thalamus but not in the midbrain, where the
complexes always contained either NR2A or NR2B, demonstrating that in
the central nervous system, different subtypes of NR2D-containing NMDA
receptors are present that vary in spatial expression, perhaps indicating distinct physiological and behavioral roles.
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